Please use this identifier to cite or link to this item: http://hdl.handle.net/2445/25209
Title: The t-SNAREs syntaxin 1 and SNAP-25 are present on organelles that participate in synaptic vesicle recycling
Author: Walch-Solimena, Christiane
Blasi Cabús, Joan
Edelmann, Lambert
Chapmann, Edwin R.
Fischer von Mollard, Gabriele
Jahn, Reinhard
Keywords: Neurones
Sinapsi
Neurotransmissió
Interacció cel·lular
Neurons
Synapses
Neural transmission
Cell interaction
Issue Date: 15-Feb-1995
Publisher: Rockefeller University Press
Abstract: Syntaxin 1 and synaptosome-associated protein of 25 kD (SNAP-25) are neuronal plasmalemma proteins that appear to be essential for exocytosis of synaptic vesicles (SVs). Both proteins form a complex with synaptobrevin, an intrinsic membrane protein of SVs. This binding is thought to be responsible for vesicle docking and apparently precedes membrane fusion. According to the current concept, syntaxin 1 and SNAP-25 are members of larger protein families, collectively designated as target-SNAP receptors (t-SNAREs), whose specific localization to subcellular membranes define where transport vesicles bind and fuse. Here we demonstrate that major pools of syntaxin 1 and SNAP-25 recycle with SVs. Both proteins cofractionate with SVs and clathrin-coated vesicles upon subcellular fractionation. Using recombinant proteins as standards for quantitation, we found that syntaxin 1 and SNAP-25 each comprise approximately 3% of the total protein in highly purified SVs. Thus, both proteins are significant components of SVs although less abundant than synaptobrevin (8.7% of the total protein). Immunoisolation of vesicles using synaptophysin and syntaxin specific antibodies revealed that most SVs contain syntaxin 1. The widespread distribution of both syntaxin 1 and SNAP-25 on SVs was further confirmed by immunogold electron microscopy. Botulinum neurotoxin C1, a toxin that blocks exocytosis by proteolyzing syntaxin 1, preferentially cleaves vesicular syntaxin 1. We conclude that t-SNAREs participate in SV recycling in what may be functionally distinct forms.
Note: Reproducció digital del document publicat a: http://dx.doi.org/10.1083/jcb.128.4.637
It is part of: Journal of Cell Biology, 1995, vol. 128, núm. 4, p. 637-645
Related resource: http://dx.doi.org/10.1083/jcb.128.4.637
URI: http://hdl.handle.net/2445/25209
ISSN: 0021-9525
Appears in Collections:Articles publicats en revistes (Patologia i Terapèutica Experimental)

Files in This Item:
File Description SizeFormat 
92437.pdf2.36 MBAdobe PDFView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.